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Q8DXM9

- GSHAB_STRA5

UniProt

Q8DXM9 - GSHAB_STRA5

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Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene
gshAB, gshF, SAG1821
Organism
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.UniRule annotation

Catalytic activityi

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.UniRule annotation
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.UniRule annotation

Cofactori

Binds 2 magnesium or manganese ions per subunit By similarity.

Enzyme regulationi

Inhibited by L-buthionine-S-sulfoximine (L-S-BSO).UniRule annotation

Kineticsi

  1. KM=22 mM for L-glutamate
  2. KM=156 µM for L-cysteine
  3. KM=8.2 mM for alpha-L-aminobutyrate
  4. KM=64 µM for ATP (in the reaction with gamma-GCS)
  5. KM=5.9 mM for gamma-L-glutamyl-L-cysteine
  6. KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate
  7. KM=6.3 mM for glycine
  8. KM=420 µM for ATP (in the reaction with GS)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi696 – 6961Magnesium or manganese 1 By similarity
Metal bindingi717 – 7171Magnesium or manganese 1 By similarity
Metal bindingi717 – 7171Magnesium or manganese 2 By similarity
Metal bindingi719 – 7191Magnesium or manganese 2 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi516 – 57459ATP By similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-cysteine ligase activity Source: UniProtKB-HAMAP
  3. glutathione synthase activity Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP
  5. manganese ion binding Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSAGA208435:GHVY-1917-MONOMER.
BRENDAi6.3.2.3. 5917.
SABIO-RKQ8DXM9.
UniPathwayiUPA00142; UER00209.
UPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione biosynthesis bifunctional protein GshAB
Alternative name(s):
Gamma-GCS-GS
Short name:
GCS-GS
Including the following 2 domains:
Glutamate--cysteine ligase (EC:6.3.2.2)
Alternative name(s):
Gamma-ECS
Short name:
GCS
Gamma-glutamylcysteine synthetase
Glutathione synthetase (EC:6.3.2.3)
Alternative name(s):
GSH synthetase
Short name:
GS
Short name:
GSH-S
Short name:
GSHase
Glutathione synthase
Gene namesi
Name:gshAB
Synonyms:gshF
Ordered Locus Names:SAG1821
OrganismiStreptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Taxonomic identifieri208435 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000821: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 750750Glutathione biosynthesis bifunctional protein GshABUniRule annotationPRO_0000192559Add
BLAST

Interactioni

Subunit structurei

Monomer Inferred.

Protein-protein interaction databases

STRINGi208435.SAG1821.

Structurei

Secondary structure

1
750
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93
Beta strandi19 – 3113
Turni32 – 354
Beta strandi44 – 463
Turni49 – 513
Beta strandi53 – 6715
Beta strandi71 – 733
Helixi74 – 9118
Beta strandi96 – 983
Beta strandi101 – 1033
Turni109 – 1113
Helixi120 – 13314
Helixi136 – 1394
Beta strandi143 – 1497
Helixi151 – 16111
Helixi166 – 19126
Beta strandi199 – 2013
Turni206 – 2083
Beta strandi212 – 2143
Beta strandi217 – 2215
Helixi234 – 24310
Turni246 – 2483
Helixi253 – 2553
Beta strandi259 – 2646
Turni268 – 2747
Beta strandi278 – 2814
Helixi296 – 31116
Helixi318 – 33417
Helixi347 – 36115
Helixi365 – 37915
Helixi381 – 3833
Helixi385 – 3928
Helixi399 – 41315
Helixi421 – 4233
Helixi428 – 44013
Beta strandi443 – 4475
Beta strandi449 – 4513
Beta strandi453 – 4586
Beta strandi461 – 4666
Turni467 – 4693
Helixi477 – 4815
Turni482 – 4843
Helixi486 – 4949
Turni507 – 5104
Helixi511 – 5177
Beta strandi518 – 5214
Beta strandi523 – 5275
Beta strandi532 – 5354
Beta strandi537 – 5415
Helixi545 – 55814
Beta strandi560 – 5667
Beta strandi570 – 5789
Beta strandi581 – 5899
Beta strandi592 – 5943
Helixi601 – 6088
Beta strandi614 – 6185
Beta strandi621 – 6233
Helixi629 – 6379
Beta strandi651 – 6544
Turni660 – 6634
Beta strandi665 – 6684
Turni670 – 6723
Helixi675 – 68713
Beta strandi694 – 7007
Beta strandi702 – 7043
Turni708 – 7114
Beta strandi714 – 7218
Helixi725 – 7284
Beta strandi731 – 7333
Helixi739 – 7468

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LN6X-ray2.95A1-750[»]
ProteinModelPortaliQ8DXM9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini489 – 747259ATP-graspAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 333333Glutamate--cysteine ligaseUniRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.
Contains 1 ATP-grasp domain.

Phylogenomic databases

eggNOGiCOG1181.
HOGENOMiHOG000156471.
KOiK01919.
OMAiHVEYVKN.
OrthoDBiEOG6BKJ7H.

Family and domain databases

Gene3Di3.30.470.20. 1 hit.
HAMAPiMF_00782. Glut_biosynth.
InterProiIPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
[Graphical view]
PfamiPF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8DXM9-1 [UniParc]FASTAAdd to Basket

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MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN    50
YHPYIQTDYS EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP 100
LSMPPKVREE DIQIAQLEDA FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG 150
QELLTSLFEL SQADNAIDFQ NQLYMKLSQN FLRYRWLLTY LYGASPVAEE 200
DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND LENAVKSGQL 250
IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD 300
TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL 350
VDAMQSVIQH FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET 400
FGQRQGQIYH DYAWEAPYAL KGYETMELST QLLLFDVIQK GVNFEVLDEQ 450
DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL AMANKVVTKK ILDEKHFPTP 500
FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK TSANLASYEK 550
AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT 600
ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT 650
KIELRRNSNI STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP 700
NATQAYSKDK KNATCIELNF NPLMYMHTYC QEGPGQSITP RILAKLFPEL 750
Length:750
Mass (Da):85,603
Last modified:March 1, 2003 - v1
Checksum:i97829C2C5B44174A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009948 Genomic DNA. Translation: AAN00684.1.
RefSeqiNP_688811.1. NC_004116.1.

Genome annotation databases

EnsemblBacteriaiAAN00684; AAN00684; SAG1821.
GeneIDi1014630.
KEGGisag:SAG1821.
PATRICi19630489. VBIStrAga72745_1829.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009948 Genomic DNA. Translation: AAN00684.1 .
RefSeqi NP_688811.1. NC_004116.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LN6 X-ray 2.95 A 1-750 [» ]
ProteinModelPortali Q8DXM9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208435.SAG1821.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN00684 ; AAN00684 ; SAG1821 .
GeneIDi 1014630.
KEGGi sag:SAG1821.
PATRICi 19630489. VBIStrAga72745_1829.

Phylogenomic databases

eggNOGi COG1181.
HOGENOMi HOG000156471.
KOi K01919.
OMAi HVEYVKN.
OrthoDBi EOG6BKJ7H.

Enzyme and pathway databases

UniPathwayi UPA00142 ; UER00209 .
UPA00142 ; UER00210 .
BioCyci SAGA208435:GHVY-1917-MONOMER.
BRENDAi 6.3.2.3. 5917.
SABIO-RK Q8DXM9.

Family and domain databases

Gene3Di 3.30.470.20. 1 hit.
HAMAPi MF_00782. Glut_biosynth.
InterProi IPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
[Graphical view ]
Pfami PF04262. Glu_cys_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-611 / 2603 V/R.
  2. "Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities."
    Janowiak B.E., Griffith O.W.
    J. Biol. Chem. 280:11829-11839(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC BAA-611 / 2603 V/R.

Entry informationi

Entry nameiGSHAB_STRA5
AccessioniPrimary (citable) accession number: Q8DXM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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